Abstract:
:Aplyronine A is a macrolide isolated from Aplysia kurodai. By monitoring fluorescent intensity of pyrenyl-actin, it was found that aplyronine A inhibited both the velocity and the degree of actin polymerization. Aplyronine A also quickly depolymerized F-actin. The kinetics of depolymerization suggest that aplyronine A severs F-actin. The relationship between the concentration of total actin and F-actin at different concentrations of aplyronine A suggests that aplyronine A forms a 1:1 complex with G-actin. From these results, it is concluded that aplyronine A inhibits actin polymerization and depolymerizes F-actin by nibbling. Comparison of the chemical structure of aplyronine A and another actin-depolymerizing macrolide, mycalolide B, suggests that the side-chain but not the macrolide ring of aplyronine A may account for its actin binding and severing activity.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Saito S,Watabe S,Ozaki H,Kigoshi H,Yamada K,Fusetani N,Karaki Hdoi
10.1093/oxfordjournals.jbchem.a021449subject
Has Abstractpub_date
1996-09-01 00:00:00pages
552-5issue
3eissn
0021-924Xissn
1756-2651journal_volume
120pub_type
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